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GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
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G-protein Coupled Receptors

G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
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G Protein-selective GPCR Conformations Measured Using FRET Sensors in a Live Cell Suspension Fluorometer Assay
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Precision vs flexibility in GPCR signaling.

Matthias Elgeti1, Alexander S Rose, Franz J Bartl

  • 1Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany. matthias.elgeti@charite.de

Journal of the American Chemical Society
|July 26, 2013
PubMed
Summary
This summary is machine-generated.

Rhodopsin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • G protein-coupled receptors (GPCRs) like rhodopsin are crucial for signal transduction.
  • Rhodopsin's light-activated state enables rapid and precise signal transmission in retinal rod cells.

Purpose of the Study:

  • To investigate the conformational dynamics of rhodopsin and its interaction with transducin.
  • To elucidate the mechanism of fast and high-fidelity signal transfer from rhodopsin to transducin.

Main Methods:

  • Fourier transform infrared (FTIR) spectroscopy to study protein conformational states.
  • All-atom molecular dynamics (MD) simulations to model rhodopsin in a membrane environment.
  • Analysis of synthetic Gtγ- and Gtα-subunit C-terminal peptides' effects on rhodopsin conformation.

Main Results:

  • FTIR revealed conserved motifs (E(D)RY and Yx7K(R)) regulate rhodopsin's inactive and active states.
  • MD simulations identified an intrinsically unstructured loop (CL3) and conformational substates.
  • GγCT stabilized active states while preserving CL3 flexibility; GαCT stabilized a helical CL3 substate.

Conclusions:

  • A mechanism for rapid, precise rhodopsin/transducin coupling is proposed, involving stepwise conformational space reduction.
  • Conserved amino acid residues play a key role in this mechanism.
  • The proposed mechanism may be generalizable to other GPCR/G protein interactions.